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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17978
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Rey, Anthony; Hocher, Antoine; Kwan, Ann; Sunde, Margaret. "Backbone and sidechain (1)H, (13)C and (15)N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae." Biomol. NMR Assignments 7, 109-112 (2013).
PubMed: 22610311
Assembly members:
MPG1, polymer, 95 residues, 9863.39 Da.
Natural source: Common Name: rice blast fungus Taxonomy ID: 318829 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Magnaporthe oryzae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHUE-MPG1
Entity Sequences (FASTA):
MPG1: SAIPAPGEGPSVSMAQQKCG
AEKVVSCCNSKELKNSKSGA
EIPIDVLSGECKNIPINILT
INQLIPINNFCSDTVSCCSG
EQIGLVNIQCTPILS
Data type | Count |
13C chemical shifts | 382 |
15N chemical shifts | 103 |
1H chemical shifts | 645 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MPG1 | 1 |
Entity 1, MPG1 95 residues - 9863.39 Da.
Residue 1 (S1) is an artifact from cloning.
1 | SER | ALA | ILE | PRO | ALA | PRO | GLY | GLU | GLY | PRO | ||||
2 | SER | VAL | SER | MET | ALA | GLN | GLN | LYS | CYS | GLY | ||||
3 | ALA | GLU | LYS | VAL | VAL | SER | CYS | CYS | ASN | SER | ||||
4 | LYS | GLU | LEU | LYS | ASN | SER | LYS | SER | GLY | ALA | ||||
5 | GLU | ILE | PRO | ILE | ASP | VAL | LEU | SER | GLY | GLU | ||||
6 | CYS | LYS | ASN | ILE | PRO | ILE | ASN | ILE | LEU | THR | ||||
7 | ILE | ASN | GLN | LEU | ILE | PRO | ILE | ASN | ASN | PHE | ||||
8 | CYS | SER | ASP | THR | VAL | SER | CYS | CYS | SER | GLY | ||||
9 | GLU | GLN | ILE | GLY | LEU | VAL | ASN | ILE | GLN | CYS | ||||
10 | THR | PRO | ILE | LEU | SER |
15N-MPG1: MPG1, [U-98% 15N], 300-400 uM; sodium phosphate 20 mM; D2O, [U-2H], 5%; H2O 95%; DSS 0.1 mM
15N13C-MPG1: MPG1, [U-98% 13C; U-98% 15N], 300-400 uM; sodium phosphate 20 mM; chloramphenicol 20 uM; complete EDTA protease cocktail tablet 0.63 mg/mL; H2O 95%; D2O, [U-99% 2H], 5%; DSS 0.1 mM
15N13C-MPG1_D2O: MPG1, [U-98% 13C; U-98% 15N], 300-400 uM; sodium phosphate 20 mM; chloramphenicol 20 uM; complete EDTA protease cocktail tablet 0.63 mg/mL; D2O, [U-99% 2H], 100%; DSS 0.1 mM
sample_conditions_1: ionic strength: 50 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 15N13C-MPG1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | 15N13C-MPG1_D2O | isotropic | sample_conditions_1 |
3D HNCACB | 15N13C-MPG1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | 15N13C-MPG1 | isotropic | sample_conditions_1 |
3D CC(CO)NH | 15N13C-MPG1 | isotropic | sample_conditions_1 |
3D HC(CO)NH | 15N13C-MPG1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 15N13C-MPG1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | 15N13C-MPG1 | isotropic | sample_conditions_1 |
3D CCH-TOCSY | 15N13C-MPG1_D2O | isotropic | sample_conditions_1 |
3D HNCO | 15N13C-MPG1 | isotropic | sample_conditions_1 |
3D HCAN | 15N13C-MPG1_D2O | isotropic | sample_conditions_1 |
3D HCA(CO)N | 15N13C-MPG1_D2O | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | 15N13C-MPG1_D2O | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | 15N13C-MPG1_D2O | isotropic | sample_conditions_1 |
TOPSPIN v2.1, Bruker Biospin - collection, processing
SPARKY v3.1, Goddard - chemical shift assignment, peak picking
TALOS vTALOS+, Cornilescu, Delaglio and Bax - data analysis
GB | AAA20128 AAX53646 AAX53647 AAX53648 AAX53649 |
REF | XP_003720513 |
SP | P52751 |
AlphaFold | P52751 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks